Homologous pairing activities of Arabidopsis thaliana RAD51 and DMC1

• Published in: Journal of biochemistry (Tokyo) 2019-03, Vol.165 (3), p.289-295
• Main Authors: Kobayashi, Wataru, Liu, Enwei, Ishii, Hajime, Matsunaga, Sachihiro, Schlögelhofer, Peter, Kurumizaka, Hitoshi
• Format: Article
• Language: English
• Subjects: Adenosine Triphosphate - metabolism; Amino Acid Sequence; Arabidopsis - metabolism; Arabidopsis Proteins - isolation & purification; Arabidopsis Proteins - metabolism; Cell Cycle Proteins - isolation & purification; Cell Cycle Proteins - metabolism; Hydrolysis; Rad51 Recombinase - isolation & purification; Rad51 Recombinase - metabolism; Rec A Recombinases - isolation & purification; Rec A Recombinases - metabolism; Sequence Alignment
• ISSN: 0021-924X; 1756-2651
• DOI: 10.1093/jb/mvy105

Abstract In eukaryotes, homologous recombination plays a pivotal role in both genome maintenance and generation of genetic diversity. Eukaryotic RecA homologues, RAD51 and DMC1, are key proteins in homologous recombination that promote pairing between homologous DNA sequences. Arabidopsis thaliana is a prominent model plant for studying eukaryotic homologous recombination. However, A. thaliana RAD51 and DMC1 have not been biochemically characterized. In the present study, we purified A. thaliana RAD51 (AtRAD51) and DMC1 (AtDMC1). Biochemical analyses revealed that both AtRAD51 and AtDMC1 possess ATP hydrolyzing activity, filament formation activity and homologous pairing activity in vitro. We then compared the homologous pairing activities of AtRAD51 and AtDMC1 with those of the Oryza sativa and Homo sapiens RAD51 and DMC1 proteins.